Dietl Andreas, Wild Klemens, Simon Bernd
European Molecular Biology Laboratory (EMBL), Structural and Computational Biology, Meyerhofstr.1, 69117, Heidelberg, Germany.
Biomol NMR Assign. 2014 Apr;8(1):93-5. doi: 10.1007/s12104-013-9460-z. Epub 2013 Jan 12.
Phosphotyrosine binding domains (PTB) are protein-protein interaction domains that play important roles in various cellular signal transduction pathways. The second phosphotyrosine binding domain (PTB2) of the human scaffolding protein FE65 interacts with the C-terminal part of the Amyloid Precursor Protein (APP) involved in Alzheimer's disease. The structure of PTB2 in complex with a 32 amino acid fragment of APP has been solved previously by X-ray crystallography. Here, we report the NMR spectral assignments of the free FE65 PTB2. This provides the basis for further investigation of the interactions of PTB2 with peptides and small organic ligands with the aim of disrupting the PTB2-APP interaction.
磷酸酪氨酸结合结构域（PTB）是蛋白质-蛋白质相互作用结构域，在各种细胞信号转导途径中发挥重要作用。人类支架蛋白FE65的第二个磷酸酪氨酸结合结构域（PTB2）与参与阿尔茨海默病的淀粉样前体蛋白（APP）的C末端部分相互作用。先前已通过X射线晶体学解析了与APP的32个氨基酸片段复合的PTB2的结构。在此，我们报告游离FE65 PTB2的核磁共振光谱归属。这为进一步研究PTB2与肽和小有机配体的相互作用奠定了基础，目的是破坏PTB2-APP相互作用。
